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http://purl.uniprot.org/citations/18390652http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18390652http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18390652http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/18390652http://www.w3.org/2000/01/rdf-schema#comment"YgaF, a protein of previously unknown function in Escherichia coli, was shown to possess noncovalently bound flavin adenine dinucleotide and to exhibit L-2-hydroxyglutarate oxidase activity. The inability of anaerobic, reduced enzyme to reverse the reaction by reducing the product alpha-ketoglutaric acid is explained by the very high reduction potential (+19 mV) of the bound cofactor. The likely role of this enzyme in the cell is to recover alpha-ketoglutarate mistakenly reduced by other enzymes or formed during growth on propionate. On the basis of the identified function, we propose that this gene be renamed lhgO."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.org/dc/terms/identifier"doi:10.1128/jb.01977-07"xsd:string
http://purl.uniprot.org/citations/18390652http://purl.org/dc/terms/identifier"doi:10.1128/jb.01977-07"xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/author"Hausinger R.P."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/author"Hausinger R.P."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/author"Mulrooney S.B."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/author"Mulrooney S.B."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/author"Kalliri E."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/author"Kalliri E."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/name"J. Bacteriol."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/pages"3793-3798"xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/pages"3793-3798"xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/title"Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/title"Identification of Escherichia coli YgaF as an L-2-hydroxyglutarate oxidase."xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/volume"190"xsd:string
http://purl.uniprot.org/citations/18390652http://purl.uniprot.org/core/volume"190"xsd:string
http://purl.uniprot.org/citations/18390652http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18390652
http://purl.uniprot.org/citations/18390652http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18390652
http://purl.uniprot.org/citations/18390652http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18390652